ID A0A397I9N8_9GLOM Unreviewed; 1433 AA.
AC A0A397I9N8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Peroxisomal ATPase PEX6 {ECO:0000256|ARBA:ARBA00034811};
DE AltName: Full=Peroxin-6 {ECO:0000256|ARBA:ARBA00034920};
GN ORFNames=Glove_242g90 {ECO:0000313|EMBL:RHZ72519.1};
OS Diversispora epigaea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Diversisporaceae; Diversispora.
OX NCBI_TaxID=1348612 {ECO:0000313|EMBL:RHZ72519.1, ECO:0000313|Proteomes:UP000266861};
RN [1] {ECO:0000313|EMBL:RHZ72519.1, ECO:0000313|Proteomes:UP000266861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IT104 {ECO:0000313|EMBL:RHZ72519.1,
RC ECO:0000313|Proteomes:UP000266861};
RA Sun X., Fei Z., Harrison M.;
RT "Genome and evolution of the arbuscular mycorrhizal fungus Diversispora
RT epigaea (formerly Glomus versiforme) and its bacterial endosymbionts.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00034440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00034440};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Peroxisome membrane
CC {ECO:0000256|ARBA:ARBA00034691}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00034691}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00034691}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RHZ72519.1}.
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DR EMBL; PQFF01000224; RHZ72519.1; -; Genomic_DNA.
DR STRING; 1348612.A0A397I9N8; -.
DR Proteomes; UP000266861; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0007031; P:peroxisome organization; IEA:UniProtKB-KW.
DR CDD; cd19527; RecA-like_PEX6_r2; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047533; RecA-like_PEX6_r2.
DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR PANTHER; PTHR23077:SF9; PEROXISOME ASSEMBLY FACTOR 2; 1.
DR Pfam; PF00004; AAA; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Peroxisome biogenesis {ECO:0000256|ARBA:ARBA00022593};
KW Reference proteome {ECO:0000313|Proteomes:UP000266861}.
FT DOMAIN 803..942
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1081..1222
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 446..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1433 AA; 160087 MW; 479F58295D44AAE8 CRC64;
METTTSFTPS TPSTPFTSSM SFIPSTSTLF TFSTPRVARI QFYDYLYTRN LKSDYRIGLS
ENLWKELIRE SDNDDENQTI LKSSICVAIT PIYSSRKNPL PKYDEKSSNL PIFSTTISYG
KYDRAPQDNI CYVSQDFAKQ NNLYNGATVE VNNANPVELD EVILGTLTYE SYELSLRDPI
TISKYFQNSS STPIIIRQGQ TYSLQNLSFT TTTTTEDDIS SFDFKVLMCN PVLQGIITDQ
TDFIITDISE DALYDIYYDD QYNLESNNLD DQNELLDQNI LDLKDDDGLN FLLANLDVVI
LGTLTYESYE LSLRDPITIS KYFQNSSSTP IIIRQGQTYS LQNLSFTTTT TTEDDISSFD
FKVLMCNPVL QGIITDQTDF IITDISEDAL YDIYYDDQYN LESNNLDDQN ELLDQNILDL
KDDDGLNFLL ANLDVGEQDQ LIEEEFERNA SVTYSSSDDD DDGDNDDENS NNENGDNNNN
NELPAPLKHS FFPIALTYPF PTNILQPIPN EKEDSESRVL VSLKELAKLG LQSGSWVLVS
GSKIEKTRMC RIYAVDVPSL IDLPLPPVYI SPVLYFNLGL GNSCFNNNIN NNNNGNDNNN
DNSGSNNNNN NNEELYIQPI MRAQFPPPIA KSISVSRIAS PHSTDRNIYN ASINGLKKWF
EDAKRIVCEG DIIPIPIDEE AARLKPQRSE GDIEEIENIH ISTKPIKLNI VVYFKVSKMN
LKNKKKCMIY GYGRQVDSKK TRLMQTGLEH SKVPVLKLYF NIVTETPSFS HINPILTAPE
TPFTKLFELI SSCLHPNATA LNLSCTVLLH GSRGCGKKTI VEWVAERVGV HVYEVNCFEF
SGETDSKTES SLRAKIDKAV TFSPCIFLLR HIDALARKSV ALETGQEPSI SSVLQDSFKQ
LLENFQTIGY PVLVIGTTGD IEKVPASVIS CFRHEISFEA PDEPTRLAIL EHLTREIPIA
PDVSLSSLAT QTAALVAKDL LDLVARAGFV AHERVKKSLI ETNKSLKDSD LVYAGIALTA
DDFNEALTKA RSSYSDSIGA PKIPNVTWDD VGGLASIKDD ILDTIQLPLE HPELFATGMK
KRSGILLYGP PGTGKTLLAK AVATSCSLNF FSVKGPELLN MYIGESEANV RRVFQRARDA
KPCVIFFDEL DSVAPKRGEK GDSGGVMDRI VSQLLAELDG MGQGGGAADV FVIGATNRPD
LLDPALLRPG RFDKLLYLGV SEDHDTQLNI IQALTRKFRL HPSLDLRSVA EKCQLNYTGA
DFYALCSDAV LKAMSRTAEK VEAKVVQLNL NPKPNLPQPV TSQYYLNHLA SLEDTLVEVT
QEDFEKALRE LVPSVSEKEL EYYRTVQMRF TQQVESKQQE MNKEESNVII NQPPPQLHPP
LEYNEQINIG VGGSSSYSYI NNNNINNNGT IEFEESPYVI DSIKKGKGKD RAE
//
